dc.contributorUniversidade Estadual Paulista (UNESP)
dc.creatorMilagre, Cíntia D. F.
dc.creatorCabeça, Luís F.
dc.creatorAlmeida, Wanda P.
dc.creatorMarsaioli, Anita J.
dc.date2014-05-27T11:26:26Z
dc.date2016-10-25T18:36:58Z
dc.date2014-05-27T11:26:26Z
dc.date2016-10-25T18:36:58Z
dc.date2012-04-02
dc.date.accessioned2017-04-06T01:58:11Z
dc.date.available2017-04-06T01:58:11Z
dc.identifierJournal of the Brazilian Chemical Society, v. 23, n. 3, p. 403-408, 2012.
dc.identifier0103-5053
dc.identifier1678-4790
dc.identifierhttp://hdl.handle.net/11449/73279
dc.identifierhttp://acervodigital.unesp.br/handle/11449/73279
dc.identifier10.1590/S0103-50532012000300005
dc.identifierS0103-50532012000300005
dc.identifier2-s2.0-84859051978.pdf
dc.identifier2-s2.0-84859051978
dc.identifierhttp://dx.doi.org/10.1590/S0103-50532012000300005
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/894096
dc.descriptionMolecular recognition events are key issues in many biological processes. STD NMR (saturation transfer difference nuclear magnetic resonance spectroscopy) is one of the techniques used to understand such biological interactions. Herein, we have investigated the interactions of four β-lactam antibiotics belonging to two classes (cephalosporins and penicillins) with human serum albumin (HSA) by 1H STD NMR revealing that the interaction between the aromatic moiety and HSA is responsible for the binding efficiency. Thus, the structural differences from the five to six-membered thio ring in penicillins and cephalosporins do not seem to influence antibiotic-albumin interactions. © 2012 Sociedade Brasileira de Química.
dc.languageeng
dc.relationJournal of the Brazilian Chemical Society
dc.rightsinfo:eu-repo/semantics/openAccess
dc.subjectβ-lactam antibiotics
dc.subjectAlbumin
dc.subjectLigand-macromolecules interaction
dc.subjectSTD NMR
dc.titleβ-lactam antibiotics epitope mapping with STD NMR spectroscopy: A study of drug-human serum albumin interaction
dc.typeOtro


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